This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4ab3
From Proteopedia
Contents |
ATP-triggered molecular mechanics of the chaperonin GroEL
Template:ABSTRACT PUBMED 22445172
Function
[CH60_ECOLI] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600]
About this Structure
4ab3 is a 14 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Clare DK, Vasishtan D, Stagg S, Quispe J, Farr GW, Topf M, Horwich AL, Saibil HR. ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin. Cell. 2012 Mar 30;149(1):113-23. Epub 2012 Mar 22. PMID:22445172 doi:10.1016/j.cell.2012.02.047
